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Database: UniProt
Entry: A0A142EQ47_9BACT
LinkDB: A0A142EQ47_9BACT
Original site: A0A142EQ47_9BACT 
ID   A0A142EQ47_9BACT        Unreviewed;       516 AA.
AC   A0A142EQ47;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   07-NOV-2018, entry version 17.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=AO498_12460 {ECO:0000313|EMBL:AMQ57252.1};
OS   Algoriphagus sp. M8-2.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=1727163 {ECO:0000313|EMBL:AMQ57252.1, ECO:0000313|Proteomes:UP000073816};
RN   [1] {ECO:0000313|Proteomes:UP000073816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8-2 {ECO:0000313|Proteomes:UP000073816};
RA   Shintani M.;
RT   "Complete sequence of Algoriphagus sp. M8-2.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMQ57252.1, ECO:0000313|Proteomes:UP000073816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8-2 {ECO:0000313|EMBL:AMQ57252.1,
RC   ECO:0000313|Proteomes:UP000073816};
RX   PubMed=27174266;
RA   Muraguchi Y., Kushimoto K., Ohtsubo Y., Suzuki T., Dohra H.,
RA   Kimbara K., Shintani M.;
RT   "Complete Genome Sequence of Algoriphagus sp. Strain M8-2, Isolated
RT   from a Brackish Lake.";
RL   Genome Announc. 4:0-0(2016).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-alpha-D-glucosidic
CC       linkages in polysaccharides containing three or more (1->4)-alpha-
CC       linked D-glucose units. {ECO:0000256|RuleBase:RU361134}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; CP012836; AMQ57252.1; -; Genomic_DNA.
DR   RefSeq; WP_067550470.1; NZ_CP012836.1.
DR   EnsemblBacteria; AMQ57252; AMQ57252; AO498_12460.
DR   KEGG; alm:AO498_12460; -.
DR   PATRIC; fig|1727163.4.peg.2606; -.
DR   KO; K01176; -.
DR   Proteomes; UP000073816; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0103025; F:alpha-amylase activity (releasing maltohexaose); IEA:UniProtKB-EC.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR022567; DUF3459.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF11941; DUF3459; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Complete proteome {ECO:0000313|Proteomes:UP000073816};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000073816}.
FT   DOMAIN       39    434       Aamy. {ECO:0000259|SMART:SM00642}.
SQ   SEQUENCE   516 AA;  59356 MW;  62DC7BBBEA83B482 CRC64;
     MNKTLITTTL TALTILASCQ SEKQPEVKNY WPQAGITYEI FVQSFNDSNG DGIGDFNGVT
     QKLDYIKELG ANAIWFMPIM PSPTYHKYDV TDYKAVHPDY GTMDDFKNLL AEAHKRDIKI
     VIDMIINHTS TEHPWFQASK SGRDSEYRDY YVWAQKDTIA DFLNKKVITL DSDNIQQWHD
     PGIGEDFYYG FFWGGMPDLN FDNPKVREEI YDIGKFWLEE VGVDGFRLDA AKHIFPDDRP
     LDNHEFWKEF RSKMVAIKPD VYLVGEVYDK KEIVAPYLPG LPALFNFDFH YTLIESLNSG
     NGQLLLQKQK EVLEFYQGIT SEFTDAIFSS NHDQPRLLND LNEDVAKYKQ ASAILLTMPG
     APYLYYGEEI GMLGLKPDEH IREPFLWDIK EKDTGRATWI EPKYSTDETV GSVEIQRNIR
     DSFFNHYKEL IRLRNSHPAL AIGSLEILEL EYPESIMAYG RKTDGQEVLV IHNVGAESME
     LNIPSEFDDV LYKLGTVEKN KESVTLGKNS TILLIK
//
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